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Structural basis for activation of zap-70 by phosphorylation of the SH2-kinase linker
Analyse Structural basis for activation of zap-70 by phosphorylation of the SH2-kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K2R
- Type
- protein
- Length
- 551 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase zap-70
- EC
- 2.7.10.2
- UniProt
- P43403
- Ligands
- ANP, MG, PO4
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase zap-70 (EC 2.7.10.2) | protein | 551 | 34% helix, 20% strand | P43403 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 495 | 0.78 | 0.86 | 55 | empty |
| 2 | 344 | 0.62 | 0.78 | 37 | MG, ANP |
| 3 | 136 | 0.60 | 0.84 | 21 | empty |
| 4 | 205 | 0.48 | 0.75 | 28 | empty |
| 5 | 51 | 0.38 | 0.81 | 17 | empty |
Compared structures
- 4K2R · Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker · the same entry in another collection · chain A against A, TM-score 1.00
- P43403 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase zap-70 (P43403) · a predicted model of the same protein · chain A against A, TM-score 0.98
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P43403
- Elsewhere: RCSB PDB 4K2R · PDBe 4K2R · UniProt P43403
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